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  1. Article ; Online: Author Correction

    Herve Celia / Istvan Botos / Xiaodan Ni / Tara Fox / Natalia de Val / Roland Lloubes / Jiansen Jiang / Susan K. Buchanan

    Communications Biology, Vol 3, Iss 1, Pp 1-

    Cryo-EM structure of the bacterial Ton motor subcomplex ExbB–ExbD provides information on structure and stoichiometry

    2020  Volume 1

    Abstract: An amendment to this paper has been published and can be accessed via a link at the top of the paper. ...

    Abstract An amendment to this paper has been published and can be accessed via a link at the top of the paper.
    Keywords Biology (General) ; QH301-705.5
    Language English
    Publishing date 2020-11-01T00:00:00Z
    Publisher Nature Publishing Group
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  2. Article ; Online: A putative ATPase mediates RNA transcription and capping in a dsRNA virus

    Xuekui Yu / Jiansen Jiang / Jingchen Sun / Z Hong Zhou

    eLife, Vol

    2015  Volume 4

    Abstract: mRNA transcription in dsRNA viruses is a highly regulated process but the mechanism of this regulation is not known. Here, by nucleoside triphosphatase (NTPase) assay and comparisons of six high-resolution (2.9–3.1 Å) cryo-electron microscopy structures ... ...

    Abstract mRNA transcription in dsRNA viruses is a highly regulated process but the mechanism of this regulation is not known. Here, by nucleoside triphosphatase (NTPase) assay and comparisons of six high-resolution (2.9–3.1 Å) cryo-electron microscopy structures of cytoplasmic polyhedrosis virus with bound ligands, we show that the large sub-domain of the guanylyltransferase (GTase) domain of the turret protein (TP) also has an ATP-binding site and is likely an ATPase. S-adenosyl-L-methionine (SAM) acts as a signal and binds the methylase-2 domain of TP to induce conformational change of the viral capsid, which in turn activates the putative ATPase. ATP binding/hydrolysis leads to an enlarged capsid for efficient mRNA synthesis, an open GTase domain for His217-mediated guanylyl transfer, and an open methylase-1 domain for SAM binding and methyl transfer. Taken together, our data support a role of the putative ATPase in mediating the activation of mRNA transcription and capping within the confines of the virus.
    Keywords viral ATPase ; histidine-mediated guanylyl transfer ; allosteric regulation ; conformational change ; Medicine ; R ; Science ; Q ; Biology (General) ; QH301-705.5
    Subject code 570
    Language English
    Publishing date 2015-08-01T00:00:00Z
    Publisher eLife Sciences Publications Ltd
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  3. Article ; Online: Cryo-EM structure of the bacterial Ton motor subcomplex ExbB–ExbD provides information on structure and stoichiometry

    Herve Celia / Istvan Botos / Xiaodan Ni / Tara Fox / Natalia De Val / Roland Lloubes / Jiansen Jiang / Susan K. Buchanan

    Communications Biology, Vol 2, Iss 1, Pp 1-

    2019  Volume 6

    Abstract: Herve Celia et al. report the single-particle cryo-EM structure of the bacterial ExbB–ExbD subcomplex reconstituted in lipid nanodiscs. They show that the ExbB pentamer encloses the ExbD dimer in the transmembrane pore, with implications for motor ... ...

    Abstract Herve Celia et al. report the single-particle cryo-EM structure of the bacterial ExbB–ExbD subcomplex reconstituted in lipid nanodiscs. They show that the ExbB pentamer encloses the ExbD dimer in the transmembrane pore, with implications for motor function.
    Keywords Biology (General) ; QH301-705.5
    Language English
    Publishing date 2019-10-01T00:00:00Z
    Publisher Nature Publishing Group
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  4. Article ; Online: Structural insight into mitochondrial β-barrel outer membrane protein biogenesis

    Kathryn A. Diederichs / Xiaodan Ni / Sarah E. Rollauer / Istvan Botos / Xiaofeng Tan / Martin S. King / Edmund R. S. Kunji / Jiansen Jiang / Susan K. Buchanan

    Nature Communications, Vol 11, Iss 1, Pp 1-

    2020  Volume 13

    Abstract: The Sorting and Assembly Machinery (SAM) complex folds beta-barrel proteins and inserts them into the mitochondrial outer membrane. Here authors report cryoEM structures of the SAM complex from Myceliophthora thermophila, which reveals a GST-like fold ... ...

    Abstract The Sorting and Assembly Machinery (SAM) complex folds beta-barrel proteins and inserts them into the mitochondrial outer membrane. Here authors report cryoEM structures of the SAM complex from Myceliophthora thermophila, which reveals a GST-like fold for Sam35 and Sam37 and sheds light on how the Sam50 beta-barrel opens a lateral gate to accommodate its substrates.
    Keywords Science ; Q
    Language English
    Publishing date 2020-07-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  5. Article ; Online: Structural insight into mitochondrial β-barrel outer membrane protein biogenesis

    Kathryn A. Diederichs / Xiaodan Ni / Sarah E. Rollauer / Istvan Botos / Xiaofeng Tan / Martin S. King / Edmund R. S. Kunji / Jiansen Jiang / Susan K. Buchanan

    Nature Communications, Vol 11, Iss 1, Pp 1-

    2020  Volume 13

    Abstract: The Sorting and Assembly Machinery (SAM) complex folds beta-barrel proteins and inserts them into the mitochondrial outer membrane. Here authors report cryoEM structures of the SAM complex from Myceliophthora thermophila, which reveals a GST-like fold ... ...

    Abstract The Sorting and Assembly Machinery (SAM) complex folds beta-barrel proteins and inserts them into the mitochondrial outer membrane. Here authors report cryoEM structures of the SAM complex from Myceliophthora thermophila, which reveals a GST-like fold for Sam35 and Sam37 and sheds light on how the Sam50 beta-barrel opens a lateral gate to accommodate its substrates.
    Keywords Science ; Q
    Language English
    Publishing date 2020-07-01T00:00:00Z
    Publisher Nature Publishing Group
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  6. Article ; Online: Structure of Human ATG9A, the Only Transmembrane Protein of the Core Autophagy Machinery

    Carlos M. Guardia / Xiao-Feng Tan / Tengfei Lian / Mitra S. Rana / Wenchang Zhou / Eric T. Christenson / Augustus J. Lowry / José D. Faraldo-Gómez / Juan S. Bonifacino / Jiansen Jiang / Anirban Banerjee

    Cell Reports, Vol 31, Iss 13, Pp 107837- (2020)

    2020  

    Abstract: Summary: Autophagy is a catabolic process involving capture of cytoplasmic materials into double-membraned autophagosomes that subsequently fuse with lysosomes for degradation of the materials by lysosomal hydrolases. One of the least understood ... ...

    Abstract Summary: Autophagy is a catabolic process involving capture of cytoplasmic materials into double-membraned autophagosomes that subsequently fuse with lysosomes for degradation of the materials by lysosomal hydrolases. One of the least understood components of the autophagy machinery is the transmembrane protein ATG9. Here, we report a cryoelectron microscopy structure of the human ATG9A isoform at 2.9-Å resolution. The structure reveals a fold with a homotrimeric domain-swapped architecture, multiple membrane spans, and a network of branched cavities, consistent with ATG9A being a membrane transporter. Mutational analyses support a role for the cavities in the function of ATG9A. In addition, structure-guided molecular simulations predict that ATG9A causes membrane bending, explaining the localization of this protein to small vesicles and highly curved edges of growing autophagosomes.
    Keywords ATG9A ; autophagosome ; autophagy ; cryo-EM ; molecular dynamics ; transmembrane protein ; Biology (General) ; QH301-705.5
    Subject code 571
    Language English
    Publishing date 2020-06-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  7. Article ; Online: Structure of the full-length TRPV2 channel by cryo-EM

    Kevin W. Huynh / Matthew R. Cohen / Jiansen Jiang / Amrita Samanta / David T. Lodowski / Z. Hong Zhou / Vera Y. Moiseenkova-Bell

    Nature Communications, Vol 7, Iss 1, Pp 1-

    2016  Volume 8

    Abstract: Transient receptor potential (TRP) proteins are Ca2+-permeable cation channels activated by a range of chemical and physical stimuli. Here the authors describe a cryo-EM structure of the full-length TRPV2 channel that provides insight into the regulation ...

    Abstract Transient receptor potential (TRP) proteins are Ca2+-permeable cation channels activated by a range of chemical and physical stimuli. Here the authors describe a cryo-EM structure of the full-length TRPV2 channel that provides insight into the regulation of the TRPV subfamily of channels.
    Keywords Science ; Q
    Language English
    Publishing date 2016-03-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  8. Article ; Online: Author Correction

    Xueni Li / Shiheng Liu / Jiansen Jiang / Lingdi Zhang / Sara Espinosa / Ryan C. Hill / Kirk C. Hansen / Z. Hong Zhou / Rui Zhao

    Nature Communications, Vol 9, Iss 1, Pp 1-

    CryoEM structure of Saccharomyces cerevisiae U1 snRNP offers insight into alternative splicing

    2018  Volume 1

    Abstract: The originally published version of this Article contained several errors in Figure 2, panel a: the basepair register in SL3-4 of yeast U1 snRNA was depicted incorrectly; the basepair for A287-U295 in yeast U1 snRNA was erroneously present; basepairs for ...

    Abstract The originally published version of this Article contained several errors in Figure 2, panel a: the basepair register in SL3-4 of yeast U1 snRNA was depicted incorrectly; the basepair for A287-U295 in yeast U1 snRNA was erroneously present; basepairs for U84-G119, G309-U532, A288-U295 and U289-A294 in yeast U1 snRNA were missing; the bulging nucleotide in SL3 of human U1 snRNA was depicted as G instead of C; and the dashed boxes defining the 5′ ss binding site and Sm site in both human and yeast snRNAs were not drawn accurately. These have now been corrected in both the PDF and HTML versions of the Article.
    Keywords Science ; Q
    Language English
    Publishing date 2018-04-01T00:00:00Z
    Publisher Nature Publishing Group
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  9. Article ; Online: CryoEM structure of the human SLC4A4 sodium-coupled acid-base transporter NBCe1

    Kevin W. Huynh / Jiansen Jiang / Natalia Abuladze / Kirill Tsirulnikov / Liyo Kao / Xuesi Shao / Debra Newman / Rustam Azimov / Alexander Pushkin / Z. Hong Zhou / Ira Kurtz

    Nature Communications, Vol 9, Iss 1, Pp 1-

    2018  Volume 9

    Abstract: Na+-coupled acid-base membrane transport proteins regulate blood pressure, ion homeostasis and acid-base chemistry. Here the authors present the 3.9 Å resolution cryoEM structure of the sodium-bicarbonate cotransporter NBCe1 and characterize its ion ... ...

    Abstract Na+-coupled acid-base membrane transport proteins regulate blood pressure, ion homeostasis and acid-base chemistry. Here the authors present the 3.9 Å resolution cryoEM structure of the sodium-bicarbonate cotransporter NBCe1 and characterize its ion coordination site and ion accessibility pathway with mutagenesis experiments.
    Keywords Science ; Q
    Language English
    Publishing date 2018-03-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  10. Article ; Online: Author Correction

    Xueni Li / Shiheng Liu / Jiansen Jiang / Lingdi Zhang / Sara Espinosa / Ryan C. Hill / Kirk C. Hansen / Z. Hong Zhou / Rui Zhao

    Nature Communications, Vol 9, Iss 1, Pp 1-

    CryoEM structure of Saccharomyces cerevisiae U1 snRNP offers insight into alternative splicing

    2018  Volume 1

    Abstract: The originally published version of this Article contained several errors in Figure 2, panel a: the basepair register in SL3-4 of yeast U1 snRNA was depicted incorrectly; the basepair for A287-U295 in yeast U1 snRNA was erroneously present; basepairs for ...

    Abstract The originally published version of this Article contained several errors in Figure 2, panel a: the basepair register in SL3-4 of yeast U1 snRNA was depicted incorrectly; the basepair for A287-U295 in yeast U1 snRNA was erroneously present; basepairs for U84-G119, G309-U532, A288-U295 and U289-A294 in yeast U1 snRNA were missing; the bulging nucleotide in SL3 of human U1 snRNA was depicted as G instead of C; and the dashed boxes defining the 5′ ss binding site and Sm site in both human and yeast snRNAs were not drawn accurately. These have now been corrected in both the PDF and HTML versions of the Article.
    Keywords Science ; Q
    Language English
    Publishing date 2018-04-01T00:00:00Z
    Publisher Nature Portfolio
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

    Full text online

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    Inter-library loan at ZB MED

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